Heme Oxygenase-1 Signaling and Redox Homeostasis in Physiopathological Conditions.

Valeria Consoli,Luca Vanella,Salvo Grosso,Valeria Sorrenti

doi:10.3390/biom11040589

Valeria Consoli, Luca Vanella + Show 2 more

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https://doi.org/10.3390/biom11040589

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Journal: Biomolecules	Publication Date: Apr 16, 2021
Citations: 106	License type: CC BY 4.0

Affiliation: University of Catania

Abstract

Heme-oxygenase is the enzyme responsible for degradation of endogenous iron protoporphyirin heme; it catalyzes the reaction’s rate-limiting step, resulting in the release of carbon monoxide (CO), ferrous ions, and biliverdin (BV), which is successively reduced in bilirubin (BR) by biliverdin reductase. Several studies have drawn attention to the controversial role of HO-1, the enzyme inducible isoform, pointing out its implications in cancer and other diseases development, but also underlining the importance of its antioxidant activity. The contribution of HO-1 in redox homeostasis leads to a relevant decrease in cells oxidative damage, which can be reconducted to its cytoprotective effects explicated alongside other endogenous mechanisms involving genes like TIGAR (TP53-induced glycolysis and apoptosis regulator), but also to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body’s antioxidant response to oxidative stress. The aim of this review was to collect most of the knowledge on HO-1 from literature, analyzing different perspectives to try and put forward a hypothesis on revealing yet unknown HO-1-involved pathways that could be useful to promote development of new therapeutical strategies, and lay the foundation for further investigation to fully understand this important antioxidant system.

Highlights

TIGAR (TP53-induced glycolysis and apoptosis regulator), and to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body’s antioxidant response to oxidative stress
Heme oxygenase (HO) is the enzyme responsible for degradation of endogenous iron protoporphyirin Heme; it catalyzes the reaction’s rate-limiting step, producing ferrous ions, carbon monoxide (CO), and biliverdin (BV), whose reduction is operated by biliverdin reductase, resulting in bilirubin (BR) formation [1]
Heme oxygenase-1 (HO-1) expression is confined to outpoured neuroglia and neurons, and there are many factors of stress that increase its induction both in neuronal and non-neuronal cells

Summary

Introduction

TIGAR (TP53-induced glycolysis and apoptosis regulator), and to the therapeutic functions of heme main transformation products, especially carbon monoxide (CO), which has been shown to be effective on GSH levels implementation sustaining body’s antioxidant response to oxidative stress. The aim of this review was to collect most of the knowledge on HO-1 from literature, analyzing different perspectives to try and put forward a hypothesis on revealing yet unknown HO-1-involved pathways that could be useful to promote development of new therapeutical strategies, and lay the foundation for further investigation to fully understand this important antioxidant system. Heme oxygenase (HO) is the enzyme responsible for degradation of endogenous iron protoporphyirin Heme; it catalyzes the reaction’s rate-limiting step, producing ferrous ions, carbon monoxide (CO), and biliverdin (BV), whose reduction is operated by biliverdin reductase, resulting in bilirubin (BR) formation [1]. The heme oxygenases are the only useful means for cell to catabolize heme, they are labeled as housekeeping genes and it is designated to control the cells heme pool [2]

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